Pressure-induced unfolding of lysozyme in aqueous guanidinium chloride solution

Protein Science

Volumn 8, Issue 7, 1999, Pages 1469-1474

  Sasahara, Kenji ^a   Nitta, Katsutoshi ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

Author keywords

Guanidinium chloride; Lysozyme; Pressure; Unfolding; Volume

Indexed keywords

GUANIDINE; LYSOZYME;

AQUEOUS SOLUTION; ARTICLE; CONCENTRATION (PARAMETERS); ENERGY TRANSFER; MOLECULAR MODEL; PRESSURE; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; STRUCTURE ACTIVITY RELATION; TEMPERATURE; ULTRAVIOLET SPECTROSCOPY;

EID: 0032813545     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.7.1469     Document Type: Article

References (38)

1. Aune KC, Tanford C. 1969. Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. 2. Dependence on denaturant concentration at 25°. Biochemistry 8:4586-4590.
2. Brandts JF, Oliveira RJ, Westort C. 1970. Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A. Biochemistry 9:1038-1047.
3. Chalikian TV, Breslauer KJ. 1996. On volume changes accompanying conformational transitions of biopolymers. Biopolymer 39:619-626.
4. Chen L, Hodgson KO, Doniach S. 1996. A lysozyme folding intermediate revealed by solution X-ray scattering. J Mol Biol 261:658-671.
5. Creighton TE. 1990. Protein folding. Biochem J 270:1-16.
6. Dewa M, Tayauchi M, Sakurai M, Nitta K. 1998. Compression refolding of cytochrome c. Protein Peptide Lett 5:265-268.
7. Dill KA, Shortle D. 1991. Denatured states of proteins. Annu Rev Biochem 60:795-825.
8. Franks F. 1995. Protein destabilization at low temperatures. Adv Protein Chem 46:105-139.
9. Frye KJ, Royer CA. 1998. Probing the contribution of internal cavities to the volume change of protein unfolding under pressure. Protein Sci 7:2217-2222.
10. Griko YV, Freire E, Privalov PL. 1994. Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study. Biochemistry 33:1889-1899.
11. Gross M, Jaenicke R. 1994. Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur J Biochem 227:617-630.
12. Haezebrouck P, Joniau M, Dael HV, Hooke SD, Woodruff ND, Dobson CM. 1995. An equilibrium partially folded state of human lysozyme at low pH. J Mol Biol 246:382-387.
13. Hawley SA. 1971. Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry 10:2436-2442.
14. Hummer G, Garde S, Garcia AE, Paulaitis ME. 1998. The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc Natl Acad Sci USA 95:1552-1555.
15. Ikeguchi M, Kuwajima K, Mitani M, Sugai S. 1986. Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme. Biochemistry 25:6965-6972.
16. Janin J. 1979. Surface and inside volumes in globular proteins. Nature 277:491-492.
17. Kauzmann W. 1959. Some factors in the interpretation of protein denaturation. Adv Protein Chem 14:1-66.
18. Kim PS, Baldwin RL. 1990. Intermediates in the folding reactions of small proteins. Annu Rev Biochem 59:631-660.
19. Kuwajima K, Hiraoka Y, Ikeguchi M, Sugai S. 1985. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry 24:874-881.
20. Lee JC, Timasheff SN. 1974. Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride. Biochemistry 13:251-265.
21. Li TM, Hook JW, Drickamer HG, Weber G. 1976. Plurality of pressure-denatured forms in chymotrypsinogen and lysozyme. Biochemistry 15:5571-5580.
22. Makhatadze GI, Privalov PL. 1992. Protein interactions with urea and guanidinium chloride. J Mol Biol 226:491-505.
23. Miranker A, Radford SE, Karplus M, Dobson CM. 1991. Demonstration by NMR of folding domains in lysozyme. Nature 349:633-636.
24. Nash DP, Jonas J. 1997. Structure of pressure-assisted cold denatured lysozyme and comparison with lysozyme folding intermediates. Biochemistry 36:14375-14383.
25. Nozaki Y. 1972. The preparation of guanidine hydrochloride. Methods Enzymol 26:43-50.
26. Privalov PL, Gill SJ. 1988. Stability of protein structure and hydrophobic interaction. Adv Protein Chem 39:191-234.
27. Privalov PL, Tiktopulo EI, Venyaminov SY, Griko YV, Makhatadze GI, Khechinashvili NN. 1989. Heat capacity and conformation of proteins in the denatured state. J Mol Biol 205:737-750.
28. Radford SE, Dobson CM, Evans PA. 1992. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 355:302-307.
29. Rose GD, Geselowitz AR, Lesser GJ, Lee RH, Zehfus MH. 1985. Hydrophobicity of amino acid residues in globular proteins. Science 229:834-838.
30. Samarasinghe SD, Campbell DM, Jonas A, Jonas J. 1992. High-resolution NMR study of the pressure-induced unfolding of lysozyme. Biochemistry 31:7773-7778.
31. Skerjanc J, Lapanje S. 1972. A dilatometric study of the denaturation of lysozyme by guanidine hydrochloride and hydrochloric acid. Eur J Biochem 25:49-53.
32. Tamura A, Kimura K, Akasaka K. 1991. Cold denaturation and heat denaturation of streptomyces subtilisin inhibitor. Biochemistry 30:11313-11320.
33. Tanford C. 1968. Protein denaturation. Adv Protein Chem 23:121-282.
34. Taniguchi Y, Suzuki K. 1983. Pressure inactivation of α-chymotrypsin. J Phys Chem 87:5185-5193.
35. Wolfenden R, Andersson L, Cullis PM, Southgate CCB. 1981. Affinities of amino acid side chains for solvent water. Biochemistry 20:849-855.
36. Yamaguchi T, Yamada H, Akasaka K. 1995. Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR. J Mol Biol 250:689-694.
37. Zhang J, Peng X, Jonas A, Jonas J. 1995. NMR study of the cold, heat, and pressure unfolding of ribonuclease A. Biochemistry 34:8631-8641.
38. Zipp A, Kauzmann W. 1973. Pressure denaturation of metmyoglobin. Biochemistry 12:4217-4228.